View source for 2ap8


==Solution structure of bombinin H4 in DPC micelles==
<StructureSection load='2ap8' size='340' side='right'caption='[[2ap8]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ap8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombina_variegata Bombina variegata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AP8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIL:D-ISOLEUCINE'>DIL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ap8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ap8 OCA], [https://pdbe.org/2ap8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ap8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ap8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ap8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BMNH5_BOMVA BMNH5_BOMVA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Skin secretions of the European frog Bombina variegata contain a family of hydrophobic peptides, called bombinins H, which probably play a role in the defense against microbes. These peptides are rich in glycine (25%), which may allow structural polymorphism. Indeed, there is increasing evidence that bombinin H can, dependent on the environment, adopt different conformations. Moreover, some of these peptides contain a d-amino acid; the bombinins H2 and H4 differ from each other in that they contain either L-Ile or D-allo-Ile at position 2. In this paper we report the solution structure obtained by using NMR techniques of the mainly helical conformation, which these peptides adopt upon binding to the bilayer mimetics SDS and DPC. A glycine ridge is exposed at one side of the helix and may provide a helix-helix interaction site. In this respect, the structure of bombinin H resembles the influenza hemagglutinin fusion peptide and the helical conformer of Alzheimer peptide Abeta(25-40). Neither structure nor orientation of bombinin H are affected by the chiral inversion. Environmental conditions can trigger self-aggregation of bombinin H in solution due to hydrophobic interaction. Under these conditions the stereochemistry of the randomly ordered N-terminal segment modulates the preference to fold into a particular conformation.

Structures of the glycine-rich diastereomeric peptides bombinin H2 and H4.,Zangger K, Gossler R, Khatai L, Lohner K, Jilek A Toxicon. 2008 Aug 1;52(2):246-54. doi: 10.1016/j.toxicon.2008.05.011. Epub 2008 , Jun 3. PMID:18586045<ref>PMID:18586045</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ap8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bombina variegata]]
[[Category: Large Structures]]
[[Category: Jilek A]]
[[Category: Khatai L]]
[[Category: Zangger K]]